Chalcogen Bonds Involving Selenium in Protein Structures

[Image: see text] Chalcogen bonds are the specific interactions involving group 16 elements as electrophilic sites. The role of chalcogen atoms as sticky sites in biomolecules is underappreciated, and the few available studies have mostly focused on S. Here, we carried out a statistical analysis ove...

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Autores principales: Carugo, Oliviero, Resnati, Giuseppe, Metrangolo, Pierangelo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8453483/
https://www.ncbi.nlm.nih.gov/pubmed/34477364
http://dx.doi.org/10.1021/acschembio.1c00441
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author Carugo, Oliviero
Resnati, Giuseppe
Metrangolo, Pierangelo
author_facet Carugo, Oliviero
Resnati, Giuseppe
Metrangolo, Pierangelo
author_sort Carugo, Oliviero
collection PubMed
description [Image: see text] Chalcogen bonds are the specific interactions involving group 16 elements as electrophilic sites. The role of chalcogen atoms as sticky sites in biomolecules is underappreciated, and the few available studies have mostly focused on S. Here, we carried out a statistical analysis over 3562 protein structures in the Protein Data Bank (PDB) containing 18 266 selenomethionines and found that Se···O chalcogen bonds are commonplace. These findings may help the future design of functional peptides and contribute to understanding the role of Se in nature.
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spelling pubmed-84534832021-09-21 Chalcogen Bonds Involving Selenium in Protein Structures Carugo, Oliviero Resnati, Giuseppe Metrangolo, Pierangelo ACS Chem Biol [Image: see text] Chalcogen bonds are the specific interactions involving group 16 elements as electrophilic sites. The role of chalcogen atoms as sticky sites in biomolecules is underappreciated, and the few available studies have mostly focused on S. Here, we carried out a statistical analysis over 3562 protein structures in the Protein Data Bank (PDB) containing 18 266 selenomethionines and found that Se···O chalcogen bonds are commonplace. These findings may help the future design of functional peptides and contribute to understanding the role of Se in nature. American Chemical Society 2021-09-03 2021-09-17 /pmc/articles/PMC8453483/ /pubmed/34477364 http://dx.doi.org/10.1021/acschembio.1c00441 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Carugo, Oliviero
Resnati, Giuseppe
Metrangolo, Pierangelo
Chalcogen Bonds Involving Selenium in Protein Structures
title Chalcogen Bonds Involving Selenium in Protein Structures
title_full Chalcogen Bonds Involving Selenium in Protein Structures
title_fullStr Chalcogen Bonds Involving Selenium in Protein Structures
title_full_unstemmed Chalcogen Bonds Involving Selenium in Protein Structures
title_short Chalcogen Bonds Involving Selenium in Protein Structures
title_sort chalcogen bonds involving selenium in protein structures
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8453483/
https://www.ncbi.nlm.nih.gov/pubmed/34477364
http://dx.doi.org/10.1021/acschembio.1c00441
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AT resnatigiuseppe chalcogenbondsinvolvingseleniuminproteinstructures
AT metrangolopierangelo chalcogenbondsinvolvingseleniuminproteinstructures

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